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Conserved domains on  [gi|9652074|gb|AAF91390|]
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arginine N-methyltransferase [Homo sapiens]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
26-199 1.92e-44

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 1.92e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   26 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 104
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074  105 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 184
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                       170
                ....*....|....*
gi 9652074  185 FDMTCIRDVAMKEPL 199
Cdd:COG4076 167 FDFRLFGFLLYAEPL 181
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
26-199 1.92e-44

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 1.92e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   26 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 104
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074  105 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 184
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                       170
                ....*....|....*
gi 9652074  185 FDMTCIRDVAMKEPL 199
Cdd:COG4076 167 FDFRLFGFLLYAEPL 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-155 5.11e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 5.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   55 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISeWMGYCLF 132
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                        90       100
                ....*....|....*....|...
gi 9652074  133 YESMLNTVIFARDKwLKPGGLMF 155
Cdd:cd02440  80 VEDLARFLEEARRL-LKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-152 2.00e-11

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     55 VLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISeWMGY 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV------DLSPEMLerareRAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVL 73

                          90       100
                  ....*....|....*....|....*
gi 9652074    130 CLFYESMLNTVI--FARdkWLKPGG 152
Cdd:pfam13649  74 HHLPDPDLEAALreIAR--VLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
47-123 1.38e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074    47 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 119
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180


                 ....
gi 9652074   120 DIII 123
Cdd:PRK00517 181 DVIV 184
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 29-154 1.43e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     29 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 102
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 9652074    103 TIFKGKVEEVELPVEKVDIIIsewMGYClfyESMLNTVIFARDKWLKPGGLM 154
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF---VGGS---GGLLQEILEAVERRLRPGGRI 118
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
26-199 1.92e-44

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 1.92e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   26 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 104
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074  105 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 184
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                       170
                ....*....|....*
gi 9652074  185 FDMTCIRDVAMKEPL 199
Cdd:COG4076 167 FDFRLFGFLLYAEPL 181
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
47-123 7.95e-13

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.51  E-value: 7.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   47 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKI----IKANHLDNIITIFKGKVeeveLPVEKVDII 122
Cdd:COG2264 144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLV 216


                .
gi 9652074  123 I 123
Cdd:COG2264 217 V 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-155 5.11e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 5.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   55 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISeWMGYCLF 132
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                        90       100
                ....*....|....*....|...
gi 9652074  133 YESMLNTVIFARDKwLKPGGLMF 155
Cdd:cd02440  80 VEDLARFLEEARRL-LKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-155 8.39e-12

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 61.57  E-value: 8.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   46 NKHVFKDKVVLDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISe 125
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC- 93

                        90       100       110
                ....*....|....*....|....*....|....
gi 9652074  126 wmGYCLFY----ESMLNTVIfardKWLKPGGLMF 155
Cdd:COG2227  94 --SEVLEHlpdpAALLRELA----RLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-152 2.00e-11

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     55 VLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISeWMGY 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV------DLSPEMLerareRAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVL 73

                          90       100
                  ....*....|....*....|....*
gi 9652074    130 CLFYESMLNTVI--FARdkWLKPGG 152
Cdd:pfam13649  74 HHLPDPDLEAALreIAR--VLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
47-123 1.38e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074    47 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 119
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180


                 ....
gi 9652074   120 DIII 123
Cdd:PRK00517 181 DVIV 184
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 55-155 4.76e-09

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 4.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   55 VLDVGSGTGILSMFAAKAGAKKVFGIecsSIS----DYSEKIIKANHLDNIITIFKGKVEEVELPvEKVDIIIS----EW 126
Cdd:COG2230  55 VLDIGCGWGGLALYLARRYGVRVTGV---TLSpeqlEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEH 130

                        90       100
                ....*....|....*....|....*....
gi 9652074  127 MGYcLFYESMLNTVifarDKWLKPGGLMF 155
Cdd:COG2230 131 VGP-ENYPAYFAKV----ARLLKPGGRLL 154
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 48-123 9.06e-09

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 55.73  E-value: 9.06e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9652074     48 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN-HLDNIITIFKGKVEEvELPVEKVDIII 123
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-155 1.00e-07

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.20  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     56 LDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMgycLFYES 135
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV---LHHVE 73

                          90       100
                  ....*....|....*....|..
gi 9652074    136 MLNTVI--FARdkWLKPGGLMF 155
Cdd:pfam08241  74 DPERALreIAR--VLKPGGILI 93
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 55-124 1.82e-07

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 51.30  E-value: 1.82e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9652074   55 VLDVGSGTGILS-MFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNIITIFKGKVEEV--ELPVEKVDIIIS 124
Cdd:COG4123  41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAaELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
50-124 4.50e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 4.50e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9652074   50 FKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKANH--LDNIITIFKGKVEEVELpVEKVDIIIS 124
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENAerLGVRVDFIRADVTRIPL-GGSVDTVVM 116
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-155 1.22e-06

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 47.30  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   51 KDKVVLDVGSGTGILSMFAAKAGAkKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISe 125
Cdd:COG2226  22 PGARVLDLGCGTGRLALALAERGA-RVTGV------DISPEMLelareRAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS- 93

                        90       100       110
                ....*....|....*....|....*....|..
gi 9652074  126 wmGYCLFYESMLNTVI--FARdkWLKPGGLMF 155
Cdd:COG2226  94 --SFVLHHLPDPERALaeIAR--VLKPGGRLV 121
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 51-123 2.04e-05

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 45.94  E-value: 2.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9652074   51 KDKVVLDVGSGTGILSMFAAKAgAKKVFGIECS--SISDySEKIIKANHLDNiITIFKGKVEEV---ELPVEKVDIII 123
Cdd:COG2265 233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpeAVED-ARENARLNGLKN-VEFVAGDLEEVlpeLLWGGRPDVVV 307
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 55-153 4.62e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 4.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   55 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISEwmgYCLF 132
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAElDPLPAESFDLVVAF---GVLH 105

                        90       100
                ....*....|....*....|...
gi 9652074  133 YESMLNTVIFARD--KWLKPGGL 153
Cdd:COG0500 106 HLPPEEREALLRElaRALKPGGV 128
PRK14968 PRK14968
putative methyltransferase; Provisional
 51-131 5.42e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 43.35  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074    51 KDKVVLDVGSGTGILSMFAAKAGaKKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVEL--PV--EKVDIII--- 123
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNG-KKVVGVD---INPYAVECAKCNAKLNNIRNNGVEVIRSDLfePFrgDKFDVILfnp 98

                         90
                 ....*....|....*....
gi 9652074   124 -----------SEWMGYCL 131
Cdd:PRK14968  99 pylpteeeeewDDWLNYAL 117
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 48-180 1.91e-04

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 41.61  E-value: 1.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   48 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN----HLDNIITIFKGKVEEV--ELPVEKVDI 121
Cdd:COG0742  38 PDIEGARVLDLFAGSGALGLEALSRGAASVVFVE---KDRKAAAVIRKNleklGLEDRARVIRGDALRFlkRLAGEPFDL 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9652074  122 IisewmgyclF---------YESMLNTVifARDKWLKPGGLM---------FPDRAALYVVaIEDRQYKDFKIHWWE 180
Cdd:COG0742 115 V---------FldppyakglLEKALELL--AENGLLAPGGLIvvehskreeLPELPAGLEL-LKERKYGDTRLSFYR 179
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-153 1.31e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.21  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   10 MTSRDY---YFDSYAHfgIHEEMLkdeVRTLTYRNSMYHNKHVF------KDKVVLDVGSGTGILSMFAAKAGaKKVFGI 80
Cdd:COG4976   1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEAPALLAEELLarlppgPFGRVLDLGCGTGLLGEALRPRG-YRLTGV 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9652074   81 ecssisDYSEKII---KANHLDniITIFKGKVEEVELPVEKVDIIISeWMGYClfYESMLNTVIFARDKWLKPGGL 153
Cdd:COG4976  75 ------DLSEEMLakaREKGVY--DRLLVADLADLAEPDGRFDLIVA-ADVLT--YLGDLAAVFAGVARALKPGGL 139
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 29-154 1.43e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     29 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 102
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 9652074    103 TIFKGKVEEVELPVEKVDIIIsewMGYClfyESMLNTVIFARDKWLKPGGLM 154
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF---VGGS---GGLLQEILEAVERRLRPGGRI 118
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 51-124 2.27e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 38.34  E-value: 2.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9652074     51 KDKVVLDVGSGTGILSMFAAKAGAKKVFGIecSSISDYSEKIIKANHLDNIIT-IFKGKVEE--VELPVEKVDIIIS 124
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGV--DLGPMQLWKPRNDPGVTFIQGdIRDPETLDllEELLGRKVDLVLS 95
arsM PRK11873
arsenite methyltransferase;
54-152 3.58e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.39  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074    54 VVLDVGSGTGILSMFAAKA-GAK-KVFGIecssisDYSEKII---KANH----LDNiITIFKGKVEEVELPVEKVDIIIS 124
Cdd:PRK11873  80 TVLDLGSGGGFDCFLAARRvGPTgKVIGV------DMTPEMLakaRANArkagYTN-VEFRLGEIEALPVADNSVDVIIS 152

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 9652074   125 ewmgyclfyesmlNTVI-FARDK---------WLKPGG 152
Cdd:PRK11873 153 -------------NCVInLSPDKervfkeafrVLKPGG 177
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
55-155 3.63e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.34  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074   55 VLDVGSGTGILS-MFAAKAGAKKVFGIecssisDYSEKIIKA--NHLDNiITIFKGKVEEVELPvEKVDIIISewmGYCL 131
Cdd:COG4106   5 VLDLGCGTGRLTaLLAERFPGARVTGV------DLSPEMLARarARLPN-VRFVVADLRDLDPP-EPFDLVVS---NAAL 73

                        90       100
                ....*....|....*....|....*...
gi 9652074  132 FY----ESMLNTVIfardKWLKPGGLMF 155
Cdd:COG4106  74 HWlpdhAALLARLA----AALAPGGVLA 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 46-153 4.52e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.04  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9652074     46 NKHVFKDKVVLDVGSGTGILSmfaaKAGAKKVFGIECSS--ISDYSEKIIKaNHLDNIITIFKGKVEEVELPVEKVDIII 123
Cdd:TIGR02072  29 EKGIFIPASVLDIGCGTGYLT----RALLKRFPQAEFIAldISAGMLAQAK-TKLSENVQFICGDAEKLPLEDSSFDLIV 103

                          90       100       110
                  ....*....|....*....|....*....|....
gi 9652074    124 S----EWMGyclfyesMLNTVIFARDKWLKPGGL 153
Cdd:TIGR02072 104 SnlalQWCD-------DLSQALSELARVLKPGGL 130
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
49-124 4.61e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.96  E-value: 4.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9652074    49 VFKDKVVLDVGSGTGILSMFAAKAgAKKVFGIEC-SSISDYSEKIIKAnhlDNIITIFKGKVEEVELPveKVDIIIS 124
Cdd:PRK14896  27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIA---AGNVEIIEGDALKVDLP--EFNKVVS 97
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
55-105 4.70e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.73  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 9652074     55 VLDVGSGTGILS-MFAAKAGAK-KVFGIECS-SISDYSEKIIKANHLDNIITIF 105
Cdd:pfam01135  77 VLEIGSGSGYLTaCFARMVGEVgRVVSIEHIpELVEIARRNLEKLGLENVIVVV 130
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 51-124 7.54e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 36.80  E-value: 7.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9652074     51 KDKVVLDVGSGTGILSMFAAKAGAKKVfgIECSSISDY----SEKIIKANHLDNiITIFKGKVEEvELPVEKVDIIIS 124
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAE--LTMVDINARalesARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIIS 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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